ID TRPG_THET8 Reviewed; 204 AA.
AC P05379; Q5SH87;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 02-NOV-2016, entry version 114.
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, GATase component;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN Name=trpG; OrderedLocusNames=TTHA1843;
OS Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2844259; DOI=10.1016/0167-4781(88)90126-1;
RA Sato S., Nakada Y., Kanaya S., Tanaka T.;
RT "Molecular cloning and nucleotide sequence of Thermus thermophilus HB8
RT trpE and trpG.";
RL Biochim. Biophys. Acta 950:303-312(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB8 / ATCC 27634 / DSM 579;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the
CC two-step biosynthesis of anthranilate, an intermediate in the
CC biosynthesis of L-tryptophan. In the first step, the glutamine-
CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides
CC the glutamine amidotransferase activity which generates ammonia as
CC a substrate that, along with chorismate, is used in the second
CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce
CC anthranilate. In the absence of TrpG, TrpE can synthesize
CC anthranilate directly from chorismate and high concentrations of
CC ammonia (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC pyruvate + L-glutamate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits:
CC a beta subunit (TrpG) and a large alpha subunit (TrpE).
CC {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00605}.
DR EMBL; X07744; CAA30567.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71666.1; -; Genomic_DNA.
DR RefSeq; WP_011228951.1; NC_006461.1.
DR RefSeq; YP_145109.1; NC_006461.1.
DR ProteinModelPortal; P05379; -.
DR STRING; 300852.TTHA1843; -.
DR MEROPS; C26.955; -.
DR EnsemblBacteria; BAD71666; BAD71666; BAD71666.
DR GeneID; 3169403; -.
DR KEGG; ttj:TTHA1843; -.
DR PATRIC; 23958655; VBITheThe93045_1814.
DR eggNOG; ENOG4105DDQ; Bacteria.
DR eggNOG; COG0512; LUCA.
DR HOGENOM; HOG000025029; -.
DR KO; K01658; -.
DR OMA; EDSTIMA; -.
DR PhylomeDB; P05379; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Glutamine amidotransferase; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1 204 Anthranilate synthase component 2.
FT /FTId=PRO_0000056902.
FT DOMAIN 13 204 Glutamine amidotransferase type-1.
FT {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT REGION 64 66 Glutamine binding.
FT {ECO:0000250|UniProtKB:P00900}.
FT REGION 141 142 Glutamine binding.
FT {ECO:0000250|UniProtKB:P00900}.
FT ACT_SITE 91 91 Nucleophile; for GATase activity.
FT {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT ACT_SITE 181 181 For GATase activity.
FT {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT ACT_SITE 183 183 For GATase activity.
FT {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT BINDING 95 95 Glutamine.
FT {ECO:0000250|UniProtKB:P00900}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 16 198 ipfam:GATase [T]
FT MYHIT 13 204 iprf:GATASE_TYPE_1 [T]
SQ SEQUENCE 204 AA; 22515 MW; 3FF4AC5FC8204C2D CRC64;
MAANGAKGRK VMRVLVVDNY DSFTYNLVQY LGELGAEPIV WRNDRFRLEE VEALDPDRIL
ISPGPCTPFE AGLSVPLVQR YAPRYPILGV CLGHQAIGAA FGGKVVPAPV LMHGKVSPIH
HDGTGVFRGL DSPFPATRYH SLAVVEVPEA LVVNAWAEEA GGRTVMGFRH RDYPTHGVQF
HPESYLTEAG KLILKNFLED PWTR
//
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